The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker
The structural maintenance of chromosome (SMC) protein complexes cohesin and condensin and the Smc5/6 complex (Smc5/6) are crucial for chromosome dynamics and stability. All contain essential ATPase domains, and cohesin and condensin interact with chromosomes through topological entrapment of DNA. H...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2015-09-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124715008268 |
| _version_ | 1828813508069818368 |
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| author | Takaharu Kanno Davide G. Berta Camilla Sjögren |
| author_facet | Takaharu Kanno Davide G. Berta Camilla Sjögren |
| author_sort | Takaharu Kanno |
| collection | DOAJ |
| description | The structural maintenance of chromosome (SMC) protein complexes cohesin and condensin and the Smc5/6 complex (Smc5/6) are crucial for chromosome dynamics and stability. All contain essential ATPase domains, and cohesin and condensin interact with chromosomes through topological entrapment of DNA. However, how Smc5/6 binds DNA and chromosomes has remained largely unknown. Here, we show that purified Smc5/6 binds DNA through a mechanism that requires ATP hydrolysis by the complex and circular DNA to be established. This also promotes topoisomerase 2-dependent catenation of plasmids, suggesting that Smc5/6 interconnects two DNA molecules using ATP-regulated topological entrapment of DNA, similar to cohesin. We also show that a complex containing an Smc6 mutant that is defective in ATP binding fails to interact with DNA and chromosomes and leads to cell death with concomitant accumulation of DNA damage when overexpressed. Taken together, these results indicate that Smc5/6 executes its cellular functions through ATP-regulated intermolecular DNA linking. |
| first_indexed | 2024-12-12T10:01:13Z |
| format | Article |
| id | doaj.art-4b07cef71188450ab917009a62ff6ba9 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-12T10:01:13Z |
| publishDate | 2015-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-4b07cef71188450ab917009a62ff6ba92022-12-22T00:27:58ZengElsevierCell Reports2211-12472015-09-011291471148210.1016/j.celrep.2015.07.048The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA LinkerTakaharu Kanno0Davide G. Berta1Camilla Sjögren2Department of Cell and Molecular Biology, Karolinska Institutet, von Eulers väg 3, 171 77 Stockholm, SwedenDepartment of Cell and Molecular Biology, Karolinska Institutet, von Eulers väg 3, 171 77 Stockholm, SwedenDepartment of Cell and Molecular Biology, Karolinska Institutet, von Eulers väg 3, 171 77 Stockholm, SwedenThe structural maintenance of chromosome (SMC) protein complexes cohesin and condensin and the Smc5/6 complex (Smc5/6) are crucial for chromosome dynamics and stability. All contain essential ATPase domains, and cohesin and condensin interact with chromosomes through topological entrapment of DNA. However, how Smc5/6 binds DNA and chromosomes has remained largely unknown. Here, we show that purified Smc5/6 binds DNA through a mechanism that requires ATP hydrolysis by the complex and circular DNA to be established. This also promotes topoisomerase 2-dependent catenation of plasmids, suggesting that Smc5/6 interconnects two DNA molecules using ATP-regulated topological entrapment of DNA, similar to cohesin. We also show that a complex containing an Smc6 mutant that is defective in ATP binding fails to interact with DNA and chromosomes and leads to cell death with concomitant accumulation of DNA damage when overexpressed. Taken together, these results indicate that Smc5/6 executes its cellular functions through ATP-regulated intermolecular DNA linking.http://www.sciencedirect.com/science/article/pii/S2211124715008268 |
| spellingShingle | Takaharu Kanno Davide G. Berta Camilla Sjögren The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker Cell Reports |
| title | The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker |
| title_full | The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker |
| title_fullStr | The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker |
| title_full_unstemmed | The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker |
| title_short | The Smc5/6 Complex Is an ATP-Dependent Intermolecular DNA Linker |
| title_sort | smc5 6 complex is an atp dependent intermolecular dna linker |
| url | http://www.sciencedirect.com/science/article/pii/S2211124715008268 |
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